Results 21 to 30 of about 11,653 (194)
Structurally distributed surface sites tune allosteric regulation
eLife, 2021 Our ability to rationally optimize allosteric regulation is limited by incomplete knowledge of the mutations that tune allostery. Are these mutations few or abundant, structurally localized or distributed?
James W McCormick +4 more
doaj +1 more source
Biophysical Journal, 2016 G-protein-coupled receptors (GPCRs) constitute a large group of integral membrane proteins that transduce extracellular signals from a wide range of agonists into targeted intracellular responses. Although the responses can vary depending on the category of G-proteins activated by a particular receptor, responses were also found to be triggered by ...
Stuart J, Edelstein +1 more
openaire +2 more sources
Probing the Regulatory Role of Allostery via Protein Dynamics of Biological Systems [PDF]
, 2023 Allostery is a universal process in cellular interaction and function. Allosteric regulation occurs when local changes from a distant site of the biomolecular structure alter the changes at the binding site. Allosteric regulation is an intrinsic property,
Souffrant, Michael G
core +1 more source
Rigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein Allostery. [PDF]
PLoS Computational Biology, 2016 Intra-protein information is transmitted over distances via allosteric processes. This ubiquitous protein process allows for protein function changes due to ligand binding events.
Robert Kalescky +3 more
doaj +1 more source
Nature Communications, 2023 Biological regulation ubiquitously depends on protein allostery, but the regulatory mechanisms are incompletely understood, especially in proteins that undergo ligand-induced allostery with few structural changes. Here we used hydrogen-deuterium exchange
Anum Glasgow +5 more
doaj +1 more source
Revealing Atomic-Level Mechanisms of Protein Allostery with Molecular Dynamics Simulations. [PDF]
PLoS Computational Biology, 2016 Molecular dynamics (MD) simulations have become a powerful and popular method for the study of protein allostery, the widespread phenomenon in which a stimulus at one site on a protein influences the properties of another site on the protein.
Samuel Hertig +2 more
doaj +1 more source
Allostery through DNA drives phenotype switching
Nature Communications, 2021 Most insights on DNA-mediated allostery upon transcription factor (TF) binding were either based on artificial promoters or found to be short-ranged. Here authors use single-molecule FRET and cryo-EM to show that Bacillus subtilis bacteria utilize long ...
Gabriel Rosenblum +5 more
doaj +1 more source
Allosteric crosstalk in modular proteins: Function fine-tuning and drug design
Computational and Structural Biotechnology Journal, 2023 Modular proteins are regulatory proteins that carry out more than one function. These proteins upregulate or downregulate a biochemical cascade to establish homeostasis in cells.
Suman Abhishek +4 more
doaj +1 more source
Role of water-bridged interactions in metal ion coupled protein allostery.
PLoS Computational Biology, 2022 Allosteric communication between distant parts of proteins controls many cellular functions, in which metal ions are widely utilized as effectors to trigger the allosteric cascade.
Xingyue Guan +4 more
doaj +1 more source
Structure-based prediction of protein allostery [PDF]
, 2018 Allostery is the functional change at one site on a protein caused by a change at a distant site. In order for the benefits of allostery to be taken advantage of, both for basic understanding of proteins and to develop new classes of drugs, the structure-
Greener, JG, Sternberg, MJE
core +4 more sources